KINETICS OF FOLDING OF THE ALL BETA-SHEET PROTEIN INTERLEUKIN-1-BETA

被引:163
作者
VARLEY, P
GRONENBORN, AM
CHRISTENSEN, H
WINGFIELD, PT
PAIN, RH
CLORE, GM
机构
[1] NIDDKD,CHEM PHYS LAB,BLDG 5,ROOM 132,BETHESDA,MD 20892
[2] UNIV NEWCASTLE UPON TYNE,DEPT BIOCHEM & GENET,NEWCASTLE TYNE NE2 4HH,ENGLAND
[3] NIH,PROT EXPRESS LAB,BETHESDA,MD 20892
关键词
D O I
10.1126/science.8493553
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The folding of the all-beta sheet protein, interleukin-1beta, was studied with nuclear magnetic resonance (NMR) spectroscopy, circular dichroism, and fluorescence. Ninety percent of the beta structure present in the native protein, as monitored by far-ultraviolet circular dichroism, was attained within 25 milliseconds, correlating with the first kinetic phase determined by tryptophan and 1-anilinonaphthalene-8-sulfonate fluorescence. In contrast, formation of stable native secondary structure, as measured by quenched-flow deuterium-hydrogen exchange experiments, began after only 1 second. Results from the NMR experiments indicated the formation of at least two intermediates with half-lives of 0.7 to 1.5 and 15 to 25 seconds. The final stabilization of the secondary structure, however, occurs on a time scale much greater than 25 seconds. These results differ from previous results on mixed alpha helix-beta sheet proteins in which both the alpha helices and beta sheets were stabilized very rapidly (less than 10 to 20 milliseconds).
引用
收藏
页码:1110 / 1113
页数:4
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